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Database: UniProt
Entry: U5BWF5_9BACT
LinkDB: U5BWF5_9BACT
Original site: U5BWF5_9BACT 
ID   U5BWF5_9BACT            Unreviewed;       342 AA.
AC   U5BWF5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   08-MAY-2019, entry version 34.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   ORFNames=P872_06955 {ECO:0000313|EMBL:ERM81869.1};
OS   Rhodonellum psychrophilum GCM71 = DSM 17998.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Rhodonellum.
OX   NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM81869.1, ECO:0000313|Proteomes:UP000016843};
RN   [1] {ECO:0000313|EMBL:ERM81869.1, ECO:0000313|Proteomes:UP000016843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GCM71 {ECO:0000313|EMBL:ERM81869.1,
RC   ECO:0000313|Proteomes:UP000016843};
RX   PubMed=24309741;
RA   Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT   "Draft Genome Sequence of the Psychrophilic and Alkaliphilic
RT   Rhodonellum psychrophilum Strain GCM71T.";
RL   Genome Announc. 1:e01014-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate +
CC         H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413,
CC         Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215;
CC         EC=6.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00281,
CC         ECO:0000256|SAAS:SAAS01124652};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00281};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00281};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS01133340}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
CC       ECO:0000256|SAAS:SAAS00089481}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS00541523}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ERM81869.1}.
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DR   EMBL; AWXR01000038; ERM81869.1; -; Genomic_DNA.
DR   RefSeq; WP_019596593.1; NZ_KB906674.1.
DR   STRING; 1123057.P872_06955; -.
DR   EnsemblBacteria; ERM81869; ERM81869; P872_06955.
DR   PATRIC; fig|1123057.7.peg.3215; -.
DR   OrthoDB; 469058at2; -.
DR   Proteomes; UP000016843; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110915, ECO:0000313|EMBL:ERM81869.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00461853};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110936};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017000};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110884};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110938};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016843}.
FT   DOMAIN      119    340       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   COILED       64     84       {ECO:0000256|SAM:Coils}.
FT   METAL       253    253       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   342 AA;  38807 MW;  08E296B830FBB67D CRC64;
     MHQDKVAEIK NAIAQATASS PEELEAYRME YISKKSVVGE LFAEMKNIPN EEKKVFGQVI
     NELKQLAEEK FQELIERVNT DKKQSNAFDI DLTLPPSNVG AGGIHPLTAT RQRIIEIFER
     IGFNLSEGPE IEDDWHNFTA LNFPINHPAR EMQDTFFIEK DPDIALRTHT SSVQVRVMEN
     QKPPIRTLSP GRVYRNEAIS ARAHCIFHQV EGLYVDENVG FADLKNTLYH FAKEMFGKET
     KVRFRPSFFP FTEPSAEIDI SCQLCGGKGC NICKGSGWVE IGGSGMVDPN VLDNCGIDSK
     KYTGFAFGMG IERIAMLKYQ IKDLRLFTEN DVRFLKQFKP ML
//
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